NGFR Protein, Human (HEK293)

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Nerve Growth Factor Receptor (NGFR) also known as CD271, p75NTR, TNFRSF16, is a transmembrane low-affinity receptor for the neurotrophin family. NGFR has no intrinsic tyrosine kinase activity. NGFR can act as a tumour suppressor, negatively regulating cell growth and proliferation. NGF-NGFR cascade activates NF-κB, leading to inhibition of apoptosis, increases survival of schwannoma, and breast cancer cells.  NGFR Protein, Human (HEK293) is a recombinant protein consisting of 222 amino acids (K29-N250) and is produced in HEK293 cells.

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  • Species: Human
  • Source: HEK293
  • Storage:
    Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
  • Biological Activity
  • Technical Parameters
  • Product Properties
  • Documentation
  • References
  • Help & FAQs

Biological Activity

Description

Nerve Growth Factor Receptor (NGFR) also known as CD271, p75NTR, TNFRSF16, is a transmembrane low-affinity receptor for the neurotrophin family. NGFR has no intrinsic tyrosine kinase activity. NGFR can act as a tumour suppressor, negatively regulating cell growth and proliferation[1]. NGF-NGFR cascade activates NF-κB, leading to inhibition of apoptosis, increases survival of schwannoma, and breast cancer cells[3].  NGFR Protein, Human (HEK293) is a recombinant protein consisting of 222 amino acids (K29-N250) and is produced in HEK293 cells.

Background

Nerve Growth Factor Receptor (NGFR) is expressed not only in nervous tissue, but also in non-neuronal normal and cancer cells, such as perivascular cells, dental pulp cells, lymphoidal follicular dendritic cells, basal epithelium of oral mucosa and hair follicles, prostate basal cells and myoepithelial cells[1].
Human NGFR shares 92.45% aa sequence identity with mouse NGFR protein and 92.42% aa sequence identity with rat NGFR protein.
Nerve Growth Factor Receptor (NGFR) is a type-I transmembrane protein, a typical structure of the TNFR superfamily and devoid of intrinsic catalytic activity. NGFR signaling involves activation of NF-kB (Rel/NF-kB transcription factors) and the phosphorylation of the transcription factor c-Jun kinase (JNK), as well as increased production of ceramide, leading to gene transcription or programmed cell death[2].
NGFR induces p53-dependent apoptosis and cell growth arrest as well as suppressed tumor growth[3]. The low-affinity nerve growth factor receptor (NGFR) p75NGFR induces apoptosis in the absence of nerve growth factor (NGF) binding but enhances neural survival when bound by NGF. NGFR enhances beta-amyloid peptide toxicity[4]. NGFR signal can induce the subsequent downregulation of melanoma antigens and eventually suppress CTL activation[5].

In Vitro

NGFR (human) knockdown induces apoptosis and inhibits p53 activation in H460 cells[3].
NGFR (human) high expression is correlated with greater regional nodal metastasis rates and poor prognosis in human oral squamous cell carcinoma[6].

Verified Bioactivity

Measured by its ability to inhibit beta-NGF-dependent proliferation of TF-1 human erythroleukemic cells. The ED50 for this effect is ≤0.58 µg/mL.

Technical Parameters

  • Species Human
  • Source HEK293
  • Tag Tag Free
  • Accession
  • Gene ID
  • Molecular Construction
    • N-term
    • NGFR (K29-N250)
      Accession # P08138-1
    • C-term
  • Protein Length

    Extracellular Domain

  • Synonyms

    NGFR; Low Affinity Neurotrophin Receptor P75NTR; Nerve Growth Factor Receptor; TNFR Superfamily, Member 16; TNFRSF16; NGF Receptor; P75NTR; Gp80-LNGFR; CD271; P75 ICD; Tumor Necrosis Factor Receptor Superfamily Member 16; Nerve Growth Factor Receptor (TNF

  • AA Sequence

    KEACPTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECVGLQSMSAPCVEADDAVCRCAYGYYQDETTGRCEACRVCEAGSGLVFSCQDKQNTVCEECPDGTYSDEANHVDPCLPCTVCEDTERQLRECTRWADAECEEIPGRWITRSTPPEGSDSTAPSTQEPEAPPEQDLIASTVAGVVTTVMGSSQPVVTRGTTDN

  • Molecular Weight

    Approximately 42-58 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

  • Glycosylation

    Yes

  • Purity

    ≥ 95%, as determined by reducing SDS-PAGE.

Product Properties

Appearance

Lyophilized powder

Formulation

1.Lyophilized from a 0.22 μm filtered solution of PBS.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.

Endotoxin Level

<0.2 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

References

Calculators

Reconstitution Calculator

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

Volume (to add to vial) Volume (to add to vial)
=
Mass (in vial) Mass (in vial)
÷
Desired Reconstitution Concentration Desired Reconstitution Concentration
Dilution Calculator

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

Concentration (start) Concentration (start)
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Volume (start) Volume (start)
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The Specific Activity Calculator Equation
  • Specific Activity (Unit/mg)
  • Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) Specific Activity (Unit/mg)
Unit/mg
= 106 ÷
Biological Activity (ED50) Biological Activity (ED50)
106 ÷
ng/mL
MOQ
Minimum order quantity
100 mg

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